Structure of a putative 2′-5′ RNA ligase from Pyrococcus horikoshii

Peter H. Rehse, Tahir H Tahirov

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Cyclic phosphodiesterase and 2′-5′ RNA ligase are members of a superfamily of proteins which share structural similarities even though their homology may be very low. A putative 2′-5′ RNA ligase from Pyrococcus horikoshii has been crystallized and its X-ray crystallographic structure determined to 2.4 Å. The protein crystallized in the orthorhombic space group P212121, with unit-cell parameters a = 44.07, b = 45.47, c = 93.17 Å and one protein monomer in the asymmetric unit. The molecular-replacement probe was a 2′-5′ RNA ligase from Thermus thermophilus which shares 30% sequence identity. The P. horikoshii RNA ligase has some structural features that have more in common with a cyclic phosphodiesterase from Arabidopsis thaliana with which it has no significant homology, yet an examination of the electrostatic surface potential clearly defines its relationship to the T. thermophilus RNA ligase. However, the size of the active-site cleft is smaller and less positively charged than that of the T. thermophilus homologue, suggesting that the actual substrate may be smaller than that previously postulated for the latter.

Original languageEnglish (US)
Pages (from-to)1207-1212
Number of pages6
JournalActa Crystallographica Section D: Biological Crystallography
Volume61
Issue number9
DOIs
StatePublished - Sep 1 2005

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Pyrococcus horikoshii
Ligases
Thermus thermophilus
homology
RNA
proteins
Type 5 Cyclic Nucleotide Phosphodiesterases
Molecular Probes
monomers
examination
Proteins
electrostatics
Phosphoric Diester Hydrolases
Static Electricity
Arabidopsis
probes
Electrostatics
Catalytic Domain
cells
Monomers

ASJC Scopus subject areas

  • Structural Biology
  • Medicine(all)

Cite this

Structure of a putative 2′-5′ RNA ligase from Pyrococcus horikoshii. / Rehse, Peter H.; Tahirov, Tahir H.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 61, No. 9, 01.09.2005, p. 1207-1212.

Research output: Contribution to journalArticle

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